The focus of this project is the development of new methods for the study of disorder and motion within protein crystals via diffuse scatter analysis. Since the Bragg peaks only represent the ordered cyrstalline structure, diffuse scattering studies investigate the lost dynamic information. The initial studies in this project have been conducted on Staphylococcal nuclease, an ideal target due to its pronounced diffuse scatter, small unit cell, and strong, high resolution diffraction. Our studies involve characterizing the diffuse scatter of Staphylococcal nuclease, quantifying its features and reproducibility, and comparing the diffuse scatter of the native crystal to that of a "perturbed" crystal, exposed to different temperatures, pressures, and solvent conditions. Once fully characterized, the diffuse scatter will be compared to theoretical models of crystalline disorder. We anticipate applying these techniques to other protein crystals. The facilities at CHESS have proven invaluable to our work, as the studies require an intense, highly collimated beam, and extremely sensitive detectors.